5ccm: Difference between revisions

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'''~~Unreleased structure~~'''

==Crystal structure of SMYD3 with SAM and EPZ030456==

~~The entry~~ 5ccm is ~~ON HOLD until Paper Publication~~

== Structural highlights ==

<table><tr><td colspan='2'>[[5ccm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCM OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCM FirstGlance].

~~Authors~~: ~~Boriack~~-~~Sjodin~~, P.A.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=4ZX:6-CHLORANYL-2-OXIDANYLIDENE-N-[(1S,5R)-8-[4-[(PHENYLMETHYL)AMINO]PIPERIDIN-1-YL]SULFONYL-8-AZABICYCLO[3.2.1]OCTAN-3-YL]-1,3-DIHYDROINDOLE-5-CARBOXAMIDE'>4ZX</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5ccl|5ccl]]</td></tr>

~~Description~~: ~~Crystal structure~~ of ~~SMYD3 with SAM~~ and ~~EPZ030456~~

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ccm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccm RCSB], [http://www.ebi.ac.uk/pdbsum/5ccm PDBsum]</td></tr>

[[Category: Boriack-Sjodin, P.A]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Histone-lysine N-methyltransferase]]

[[Category: Boriack-Sjodin, P A]]

[[Category: Drug discovery]]

[[Category: Epigenetic]]

[[Category: Methyltransferase]]

[[Category: Protein-inhibitor complex]]

[[Category: Transferase-transferase inhibitor complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of SMYD3 with SAM and EPZ030456==
+<StructureSection load='5ccm' size='340' side='right' caption='[[5ccm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-The entry 5ccm is ON HOLD  until Paper Publication
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5ccm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CCM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CCM FirstGlance]. <br>
-Authors: Boriack-Sjodin, P.A.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4ZX:6-CHLORANYL-2-OXIDANYLIDENE-N-[(1S,5R)-8-[4-[(PHENYLMETHYL)AMINO]PIPERIDIN-1-YL]SULFONYL-8-AZABICYCLO[3.2.1]OCTAN-3-YL]-1,3-DIHYDROINDOLE-5-CARBOXAMIDE'>4ZX</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ccl|5ccl]]</td></tr>
-Description: Crystal structure of SMYD3 with SAM and EPZ030456
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ccm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ccm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5ccm RCSB], [http://www.ebi.ac.uk/pdbsum/5ccm PDBsum]</span></td></tr>
-[[Category: Boriack-Sjodin, P.A]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Histone-lysine N-methyltransferase]]
+[[Category: Boriack-Sjodin, P A]]
+[[Category: Drug discovery]]
+[[Category: Epigenetic]]
+[[Category: Methyltransferase]]
+[[Category: Protein-inhibitor complex]]
+[[Category: Transferase-transferase inhibitor complex]]